Resonance Raman Spectroscopic Study of Cytochrome c Mutants

Abstract

Abstract: The spectroscopic characteristics of cytochrome c(WT) and its mutants(Y67F and N52I) in the low frequency region were studied by Resonance Raman technique. The results show that the replacement of phenylalanine for Tyr 67 in WThad a very slight effect on the hydrogen bonding and conformation of the amino acid residues around propionic acid side chains of heme group. However, large effects on the hydrogen bonding of internal water with its surrounding amino acid residues and hydrophobility of the heme cavity were observed as Asn52 was substituted with isoleucine, which resulted in conformational regulations of heme group and surrounding amino acid residues.

Key words: Cytochrome c, Mutation, Resonance Raman spectroscopy, Amino acid conformation

CLC Number:

O657.37

TrendMD:

ZHENG Jun-Wei, GU Ren-Ao, LU Tian-Hong. Resonance Raman Spectroscopic Study of Cytochrome c Mutants[J]. Chem. J. Chinese Universities, 2002, 23(1): 42.

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Resonance Raman Spectroscopic Study of Cytochrome c Mutants

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